Journal
NUCLEIC ACIDS RESEARCH
Volume 28, Issue 15, Pages 2866-2872Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/28.15.2866
Keywords
-
Categories
Ask authors/readers for more resources
The amino acid sequence of human cytoplasmic cysteinyl-tRNA synthetase (CRS) was examined by analyzing sequences of genomic and expressed sequence tag fragments. From theses analyses, a few interesting possibilities were suggested for the structure of human CRS, First, different isoforms of CRS may result from alternative splicing, Second, the largest one would comprise 831 amino acids, Third, a new exon was identified encoding an 83 amino acid domain that is homologous to parts of elongation factor-1 subunits as well as other proteins involved in protein synthesis, Northern blot analysis showed three different mRNAs for CRS (of similar to 3.0, 2.7 and 2.0 kb) from human testis while only the 2.7 kb mRNA was commonly detected in other tissues. Expression of the exon 2-containing transcript in testis was confirmed by RT-PCR and northern blotting, CRS containing the exon 2-encoded peptide retained catalytic activity comparable to that lacking this peptide. This peptide was responsible for the specific interaction of CRS with elongation factor-1 gamma.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available